The objective of this work is to determine the structure of saccharide complexes with concanavalin A in solution. The method which will be used involves the measurement of the C13 relaxation rates of individual carbon atoms of the saccharides (Beta-methyl-maltoside, sucrose and metizitose) by nuclear magnetic resonance. These studies will take advantage of the dipolar relaxation effect between C13 and the protein- bound paramagnetic metal ion Mn(II) to obtain distances between C13 and MN(II). The structure of the saccharide-concanavalin A complexes can then be determined. These studies are of paramount importance in understanding the nature and specificity of concanavalin A binding to cell wall polysaccharides. The important finding that concanavalin A can agglutinate leukemic cells which have been transformed by polyoma virus, chemical carcinogens, and irradiation by x-rays but does not agglutinate normal cells has prompted us to study the fundamental nature of the saccharide - concanavalin A structural interactions. Knowledge of the specificity in binding a concanavalin A to the membrane receptor sites may prove useful in understanding malignancy. The nuclear magnetic resonance studies which we propose will compliment the x-ray structural work done on this protein since the x-ray work has not been able to provide structural information on saccharide-protein complexes.